Metabolic Modeling Tutorial
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Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
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Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
12/28 - 12/31
for maintenance.
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
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for maintenance.
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
12/28 - 12/31
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Aquifex aeolicus VF5 Reaction: 4.2.1.122

Superclasses: Reactions Classified By Conversion Type Simple Reactions Chemical Reactions
Reactions Classified By Substrate Small-Molecule Reactions

EC Number: 4.2.1.122

Enzymes and Genes:
tryptophan synthase subunit beta : trpB1
tryptophan synthase subunit beta : trpB2

Sub-reaction of:
4.2.1.20: (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = L-tryptophan + D-glyceraldehyde 3-phosphate + H2O

In Pathway: tryptophan biosynthesis

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

Mass balance status: Balanced.

Enzyme Commission Primary Name: tryptophan synthase (indole-salvaging)

Enzyme Commission Synonyms: tryptophan synthase β2

Standard Gibbs Free Energy (ΔrG in kcal/mol): -15.4869995 Inferred by computational analysis [Latendresse13]

Enzyme Commission Summary:
Most mesophilic bacteria have a multimeric tryptophan synthase complex (EC 4.2.1.20) that forms L-tryptophan from L-serine and 1-C-(indol-3-yl)glycerol 3-phosphate via an indole intermediate. This intermediate, which is formed by the α subunits, is transferred in an internal tunnel to the β units, which convert it to tryptophan. In thermophilic organisms the high temperature enhances diffusion and causes the loss of indole. This enzyme, which does not combine with the α unit to form a complex, salvages the lost indole back to L-tryptophan. It has a much lower Km for indole than the β subunit of EC 4.2.1.20.

Citations: [Hettwer02, Yee96]

Gene-Reaction Schematic: ?

Relationship Links: BRENDA:EC:4.2.1.122 , ENZYME:EC:4.2.1.122 , IUBMB-ExplorEnz:EC:4.2.1.122

Credits:
Revised in MetaCyc 09-Apr-2011 by Caspi R , SRI International
Imported from MetaCyc 08-Aug-2014 by Subhraveti P , SRI International


References

Hettwer02: Hettwer S, Sterner R (2002). "A novel tryptophan synthase beta-subunit from the hyperthermophile Thermotoga maritima. Quaternary structure, steady-state kinetics, and putative physiological role." J Biol Chem 277(10);8194-201. PMID: 11756459

Latendresse13: Latendresse M. (2013). "Computing Gibbs Free Energy of Compounds and Reactions in MetaCyc."

Yee96: Yee MC, Horn V, Yanofsky C (1996). "On the role of helix 0 of the tryptophan synthetase alpha chain of Escherichia coli." J Biol Chem 271(25);14754-63. PMID: 8662916


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Page generated by SRI International Pathway Tools version 18.5 on Sun Dec 21, 2014, biocyc14.